ID F7V798_CLOSS Unreviewed; 202 AA.
AC F7V798;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE RecName: Full=Urease accessory protein UreG {ECO:0000256|HAMAP-Rule:MF_01389};
GN Name=HypB {ECO:0000313|EMBL:BAK48526.1};
GN Synonyms=ureG {ECO:0000256|HAMAP-Rule:MF_01389};
GN OrderedLocusNames=CXIVA_25570 {ECO:0000313|EMBL:BAK48526.1};
OS Clostridium sp. (strain SY8519).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1042156 {ECO:0000313|EMBL:BAK48526.1, ECO:0000313|Proteomes:UP000008937};
RN [1] {ECO:0000313|Proteomes:UP000008937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SY8519 {ECO:0000313|Proteomes:UP000008937};
RX PubMed=21914882; DOI=10.1128/JB.05637-11;
RA Yokoyama S., Oshima K., Nomura I., Hattori M., Suzuki T.;
RT "Complete genomic sequence of the O-desmethylangolensin-producing bacterium
RT Clostridium rRNA cluster XIVa strain SY8519, isolated from adult human
RT intestine.";
RL J. Bacteriol. 193:5568-5569(2011).
CC -!- FUNCTION: Facilitates the functional incorporation of the urease nickel
CC metallocenter. This process requires GTP hydrolysis, probably
CC effectuated by UreG. {ECO:0000256|HAMAP-Rule:MF_01389}.
CC -!- SUBUNIT: Homodimer. UreD, UreF and UreG form a complex that acts as a
CC GTP-hydrolysis-dependent molecular chaperone, activating the urease
CC apoprotein by helping to assemble the nickel containing metallocenter
CC of UreC. The UreE protein probably delivers the nickel.
CC {ECO:0000256|HAMAP-Rule:MF_01389}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389}.
CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. UreG
CC subfamily. {ECO:0000256|ARBA:ARBA00005732, ECO:0000256|HAMAP-
CC Rule:MF_01389}.
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DR EMBL; AP012212; BAK48526.1; -; Genomic_DNA.
DR RefSeq; WP_013978479.1; NC_015737.1.
DR AlphaFoldDB; F7V798; -.
DR STRING; 1042156.CXIVA_25570; -.
DR KEGG; cls:CXIVA_25570; -.
DR eggNOG; COG0378; Bacteria.
DR HOGENOM; CLU_072144_1_0_9; -.
DR OrthoDB; 9802035at2; -.
DR Proteomes; UP000008937; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006807; P:nitrogen compound metabolic process; IEA:InterPro.
DR CDD; cd05540; UreG; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_01389; UreG; 1.
DR InterPro; IPR003495; CobW/HypB/UreG_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR004400; UreG.
DR NCBIfam; TIGR00101; ureG; 1.
DR PANTHER; PTHR31715; UREASE ACCESSORY PROTEIN G; 1.
DR PANTHER; PTHR31715:SF0; UREASE ACCESSORY PROTEIN G; 1.
DR Pfam; PF02492; cobW; 1.
DR PIRSF; PIRSF005624; Ni-bind_GTPase; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|HAMAP-Rule:MF_01389};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_01389};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_01389};
KW Nickel insertion {ECO:0000256|ARBA:ARBA00022988, ECO:0000256|HAMAP-
KW Rule:MF_01389};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_01389}; Reference proteome {ECO:0000313|Proteomes:UP000008937}.
FT DOMAIN 6..176
FT /note="CobW/HypB/UreG nucleotide-binding"
FT /evidence="ECO:0000259|Pfam:PF02492"
FT BINDING 10..17
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01389"
SQ SEQUENCE 202 AA; 22211 MW; 9F29A43ABB96AB1E CRC64;
MSYVKIGVAG PVGSGKTALI EALTREMAKD YSIGVITNDI YTKEDAEFLS KNSVLPMERI
IGVETGGCPH TAIREDASMN LEAVDEMMER FPDIELLFIE SGGDNLSATF SPELVEATIF
VIDVAEGDKI PRKGGPGITR SDLLVINKID LAPYVGADLG VMERDSRKMR GDRPFLFTNI
RDREGVDQVI RWIKENVLLE GC
//